node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
Mmc1_1437 | glyQ | Mmc1_1437 | Mmc1_1440 | KEGG: pca:Pcar_1232 HD domain protein; TIGRFAM: metal dependent phophohydrolase; PFAM: metal-dependent phosphohydrolase, HD sub domain; metal-dependent phosphohydrolase, 7TM intracellular region; SMART: metal-dependent phosphohydrolase, HD region. | PFAM: glycyl-tRNA synthetase, alpha subunit; KEGG: pca:Pcar_0598 glycyl-tRNA synthetase, alpha subunit. | 0.750 |
Mmc1_1437 | glyS | Mmc1_1437 | Mmc1_1441 | KEGG: pca:Pcar_1232 HD domain protein; TIGRFAM: metal dependent phophohydrolase; PFAM: metal-dependent phosphohydrolase, HD sub domain; metal-dependent phosphohydrolase, 7TM intracellular region; SMART: metal-dependent phosphohydrolase, HD region. | KEGG: yps:YPTB3916 glycyl-tRNA synthetase beta subunit. | 0.750 |
Mmc1_1437 | lnt | Mmc1_1437 | Mmc1_1439 | KEGG: pca:Pcar_1232 HD domain protein; TIGRFAM: metal dependent phophohydrolase; PFAM: metal-dependent phosphohydrolase, HD sub domain; metal-dependent phosphohydrolase, 7TM intracellular region; SMART: metal-dependent phosphohydrolase, HD region. | Apolipoprotein N-acyltransferase; Catalyzes the phospholipid dependent N-acylation of the N- terminal cysteine of apolipoprotein, the last step in lipoprotein maturation; Belongs to the CN hydrolase family. Apolipoprotein N- acyltransferase subfamily. | 0.765 |
Mmc1_1437 | ybeY | Mmc1_1437 | Mmc1_1438 | KEGG: pca:Pcar_1232 HD domain protein; TIGRFAM: metal dependent phophohydrolase; PFAM: metal-dependent phosphohydrolase, HD sub domain; metal-dependent phosphohydrolase, 7TM intracellular region; SMART: metal-dependent phosphohydrolase, HD region. | Protein of unknown function UPF0054; Single strand-specific metallo-endoribonuclease involved in late-stage 70S ribosome quality control and in maturation of the 3' terminus of the 16S rRNA. | 0.833 |
alaS | aspS | Mmc1_0013 | Mmc1_0942 | alanyl-tRNA synthetase; Catalyzes the attachment of alanine to tRNA(Ala) in a two- step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged Ser-tRNA(Ala) and Gly-tRNA(Ala) via its editing domain. | aspartyl-tRNA synthetase; Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn); Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily. | 0.909 |
alaS | glyQ | Mmc1_0013 | Mmc1_1440 | alanyl-tRNA synthetase; Catalyzes the attachment of alanine to tRNA(Ala) in a two- step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged Ser-tRNA(Ala) and Gly-tRNA(Ala) via its editing domain. | PFAM: glycyl-tRNA synthetase, alpha subunit; KEGG: pca:Pcar_0598 glycyl-tRNA synthetase, alpha subunit. | 0.718 |
alaS | glyS | Mmc1_0013 | Mmc1_1441 | alanyl-tRNA synthetase; Catalyzes the attachment of alanine to tRNA(Ala) in a two- step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged Ser-tRNA(Ala) and Gly-tRNA(Ala) via its editing domain. | KEGG: yps:YPTB3916 glycyl-tRNA synthetase beta subunit. | 0.701 |
alaS | ileS | Mmc1_0013 | Mmc1_2147 | alanyl-tRNA synthetase; Catalyzes the attachment of alanine to tRNA(Ala) in a two- step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged Ser-tRNA(Ala) and Gly-tRNA(Ala) via its editing domain. | Isoleucyl-tRNA synthetase; Catalyzes the attachment of isoleucine to tRNA(Ile). As IleRS can inadvertently accommodate and process structurally similar amino acids such as valine, to avoid such errors it has two additional distinct tRNA(Ile)-dependent editing activities. One activity is designated as 'pretransfer' editing and involves the hydrolysis of activated Val-AMP. The other activity is designated 'posttransfer' editing and involves deacylation of mischarged Val-tRNA(Ile). Belongs to the class-I aminoacyl-tRNA synthetase family. IleS type 1 subfamily. | 0.793 |
alaS | leuS | Mmc1_0013 | Mmc1_0432 | alanyl-tRNA synthetase; Catalyzes the attachment of alanine to tRNA(Ala) in a two- step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged Ser-tRNA(Ala) and Gly-tRNA(Ala) via its editing domain. | TIGRFAM: leucyl-tRNA synthetase; KEGG: pca:Pcar_1413 leucyl-tRNA synthetase; Belongs to the class-I aminoacyl-tRNA synthetase family. | 0.830 |
alaS | pheT | Mmc1_0013 | Mmc1_0368 | alanyl-tRNA synthetase; Catalyzes the attachment of alanine to tRNA(Ala) in a two- step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged Ser-tRNA(Ala) and Gly-tRNA(Ala) via its editing domain. | TIGRFAM: phenylalanyl-tRNA synthetase, beta subunit; KEGG: pca:Pcar_1423 phenylalanyl-tRNA synthetase, beta subunit. | 0.922 |
alaS | valS | Mmc1_0013 | Mmc1_1474 | alanyl-tRNA synthetase; Catalyzes the attachment of alanine to tRNA(Ala) in a two- step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged Ser-tRNA(Ala) and Gly-tRNA(Ala) via its editing domain. | valyl-tRNA synthetase; Catalyzes the attachment of valine to tRNA(Val). As ValRS can inadvertently accommodate and process structurally similar amino acids such as threonine, to avoid such errors, it has a 'posttransfer' editing activity that hydrolyzes mischarged Thr-tRNA(Val) in a tRNA- dependent manner; Belongs to the class-I aminoacyl-tRNA synthetase family. ValS type 1 subfamily. | 0.896 |
aspS | alaS | Mmc1_0942 | Mmc1_0013 | aspartyl-tRNA synthetase; Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn); Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily. | alanyl-tRNA synthetase; Catalyzes the attachment of alanine to tRNA(Ala) in a two- step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged Ser-tRNA(Ala) and Gly-tRNA(Ala) via its editing domain. | 0.909 |
aspS | glyQ | Mmc1_0942 | Mmc1_1440 | aspartyl-tRNA synthetase; Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn); Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily. | PFAM: glycyl-tRNA synthetase, alpha subunit; KEGG: pca:Pcar_0598 glycyl-tRNA synthetase, alpha subunit. | 0.641 |
aspS | glyS | Mmc1_0942 | Mmc1_1441 | aspartyl-tRNA synthetase; Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn); Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily. | KEGG: yps:YPTB3916 glycyl-tRNA synthetase beta subunit. | 0.693 |
aspS | ileS | Mmc1_0942 | Mmc1_2147 | aspartyl-tRNA synthetase; Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn); Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily. | Isoleucyl-tRNA synthetase; Catalyzes the attachment of isoleucine to tRNA(Ile). As IleRS can inadvertently accommodate and process structurally similar amino acids such as valine, to avoid such errors it has two additional distinct tRNA(Ile)-dependent editing activities. One activity is designated as 'pretransfer' editing and involves the hydrolysis of activated Val-AMP. The other activity is designated 'posttransfer' editing and involves deacylation of mischarged Val-tRNA(Ile). Belongs to the class-I aminoacyl-tRNA synthetase family. IleS type 1 subfamily. | 0.704 |
aspS | leuS | Mmc1_0942 | Mmc1_0432 | aspartyl-tRNA synthetase; Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn); Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily. | TIGRFAM: leucyl-tRNA synthetase; KEGG: pca:Pcar_1413 leucyl-tRNA synthetase; Belongs to the class-I aminoacyl-tRNA synthetase family. | 0.683 |
aspS | pheT | Mmc1_0942 | Mmc1_0368 | aspartyl-tRNA synthetase; Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn); Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily. | TIGRFAM: phenylalanyl-tRNA synthetase, beta subunit; KEGG: pca:Pcar_1423 phenylalanyl-tRNA synthetase, beta subunit. | 0.853 |
aspS | valS | Mmc1_0942 | Mmc1_1474 | aspartyl-tRNA synthetase; Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn); Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily. | valyl-tRNA synthetase; Catalyzes the attachment of valine to tRNA(Val). As ValRS can inadvertently accommodate and process structurally similar amino acids such as threonine, to avoid such errors, it has a 'posttransfer' editing activity that hydrolyzes mischarged Thr-tRNA(Val) in a tRNA- dependent manner; Belongs to the class-I aminoacyl-tRNA synthetase family. ValS type 1 subfamily. | 0.883 |
glyQ | Mmc1_1437 | Mmc1_1440 | Mmc1_1437 | PFAM: glycyl-tRNA synthetase, alpha subunit; KEGG: pca:Pcar_0598 glycyl-tRNA synthetase, alpha subunit. | KEGG: pca:Pcar_1232 HD domain protein; TIGRFAM: metal dependent phophohydrolase; PFAM: metal-dependent phosphohydrolase, HD sub domain; metal-dependent phosphohydrolase, 7TM intracellular region; SMART: metal-dependent phosphohydrolase, HD region. | 0.750 |
glyQ | alaS | Mmc1_1440 | Mmc1_0013 | PFAM: glycyl-tRNA synthetase, alpha subunit; KEGG: pca:Pcar_0598 glycyl-tRNA synthetase, alpha subunit. | alanyl-tRNA synthetase; Catalyzes the attachment of alanine to tRNA(Ala) in a two- step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged Ser-tRNA(Ala) and Gly-tRNA(Ala) via its editing domain. | 0.718 |